Science · 1987 · 133 citations · 20 references
Peptide EngineeringMolecular BiologyPeptide SciencePeptide ChemistryProtein FoldingAmino TerminusSequence-specific Dna-cleaving PeptideBiochemistrySynthetic 52-Residue PeptideBioconjugationDna ReplicationStructural BiologyNatural SciencesPeptide LibrarySynthetic BiologyPeptide SynthesisProtein EngineeringMedicineHybrid Peptide
A synthetic 52-residue peptide based on the sequence-specific DNA-binding domain of Hin recombinase (139-190) has been equipped with ethylenediaminetetraacetic acid (EDTA) at the amino terminus. In the presence of Fe(II), this synthetic EDTA-peptide cleaves DNA at Hin recombination sites. The cleavage data reveal that the amino terminus of Hin(139-190) is bound in the minor groove of DNA near the symmetry axis of Hin recombination sites. This work demonstrates the construction of a hybrid peptide combining two functional domains: sequence-specific DNA binding and DNA cleavage.
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J. Garnier, David J. Osguthorpe, Barry Robson · Journal of Molecular Biology · 1978 · 4.6K citations
Structural Bioinformatics, Biomolecular Structure Prediction, Protein Folding +13
Design of Sequence-Specific DNA-Binding Molecules
Peter B. Dervan · Science · 1986 · 837 citations
Structure of the cro repressor from bacteriophage λ and its interaction with DNA
W.F. Anderson, D.H. Ohlendorf, Yoshinori Takeda et al. · Nature · 1981 · 547 citations